Please sign in to continue.
Molecular mechanism of the Hofmeister series · revision history
Revision 1
Superseded · first revision · record
- Title
- Molecular mechanism of the Hofmeister series
- Plain
- Since 1888 it has been known that salts fall in a fixed order, the Hofmeister series, in how strongly they make proteins precipitate. Why ions of the same charge rank this way is still debated.
- Precise
- Explain the anion ordering of the Hofmeister series (roughly SO4^2- > F- > Cl- > Br- > NO3- > I- > ClO4- > SCN-) in protein salting-out, nonpolar solute solubility and electrolyte surface tension, choosing among bulk water structure making and breaking, direct ion-solute pairing, interfacial adsorption driven by polarizability and partial dehydration, and ion-specific dispersion forces. An answer is a quantitative model with parameters from first principles or independent data that reproduces the ordering and its reversal on positively charged or hydrophobic surfaces.
- Settled by
- Ion-resolved measurements at protein and model interfaces compared with simulations using polarizable or ab initio potentials across the whole series.
- Kind
- phenomenon
- Answer type
- mechanism
- References
- (empty)
- Literature status
- contested
- Status note
- Explanations based on bulk water structure lost support in the 2000s in favor of direct ion-interface interactions, but no single quantitative model covers the series (Jungwirth and Cremer, Nature Chemistry 2014, https://doi.org/10.1038/nchem.1899).
- Posed since
- 1888